Reversible peptide oligomerization over nanoscale gold surfaces

Kazushige Yokoyama; Christa D. Catalfamo; Minxuan Yuan

doi:10.3934/biophy.2015.4.649

AIMS Biophysics, 2015, 2(4): 649-665. doi: 10.3934/biophy.2015.4.649. Review Special Issues

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Reversible peptide oligomerization over nanoscale gold surfaces

Kazushige Yokoyama, Christa D. Catalfamo, Minxuan Yuan

Department of Chemistry, State University of New York Geneseo College, 14454 Geneseo, NY 14454, USA

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Special Issues: Protein folding or molecular self-assembly over nanoscale surface

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A selective oligomeric formation of amyloid beta 1-40 (Ab_1-40) monomers over a nanogold colloidal surface was investigated. An unfolded Ab_1-40 monomer is considered to construct a dimer or trimer based oligomeric form with its hydrophobic segment placing outward under an acidic condition. Under a basic condition, a conformation of Ab is expected to take a folded monomeric form with its hydrophilic segment folded inward, avoiding the networking with residual colloidal particles. The most probable oligomeric form constructed over a 20 nm gold colloidal surface within a 25 ℃ to 65 ℃ temperature range is a dimer based unit and that over 30 or 40 nm gold colloidal surface below 15 ℃ is concluded to be a trimer based unit. However, selective oligomerization was not successfully reproduced under the rest of the conditions. A dipole-induced dipole interaction must cause a flexible structural change between folded and unfolded forms.

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Keywords: amyloid beta; protein folding; nanoparticles; self-assembly; oligomers

Citation: Kazushige Yokoyama, Christa D. Catalfamo, Minxuan Yuan. Reversible peptide oligomerization over nanoscale gold surfaces. AIMS Biophysics, 2015, 2(4): 649-665. doi: 10.3934/biophy.2015.4.649

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